ArticlePloS one2015
Modulation of the Activity of Mycobacterium tuberculosis LipY by Its PE Domain.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The trial behind it
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- TargetingRSC medicinal chemistry · 2023Review
- Article
- Evaluation of the Impact of Esterases and Lipases from the Circulatory System against Substrates of Different Lipophilicity.International journal of molecular sciences · 2022Article
- The structure of helical lipoprotein lipase reveals an unexpected twist in lipase storage.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Type VII Secretion Substrates of Pathogenic Mycobacteria Are Processed by a Surface Protease.mBio · 2019Article
- Optimization of secretion and surface localization of heterologous OVA protein in mycobacteria by using LipY as a carrier.Microbial cell factories · 2019Article
- Microbial esterases and ester prodrugs: An unlikely marriage for combating antibiotic resistance.Drug development research · 2019Review
- Delineating the Physiological Roles of the PE and Catalytic Domains of LipY in Lipid Consumption in Mycobacterium-Infected Foamy Macrophages.Infection and immunity · 2018Article
- Biochemical Analysis of the Lipoprotein Lipase Truncation Variant, LPLBiochemistry · 2017Article
- Prediction of Certain Well-Characterized Domains of Known Functions within the PE and PPE Proteins of Mycobacteria.PloS one · 2016Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Mycobacterium tuberculosis harbors over 160 genes encoding PE/PPE proteins, several of which have roles in the pathogen's virulence. A number of PE/PPE proteins are secreted via Type VII secretion systems known as the ESX secretion systems. One PE protein, LipY, has a triglyceride lipase domain in addition to its PE domain. LipY can regulate intracellular triglyceride levels and is also exported to the cell wall by one of the ESX family members, ESX-5. Upon export, LipY's PE domain is removed by proteolytic cleavage. Studies using cells and crude extracts suggest that LipY's PE domain not only directs its secretion by ESX-5, but also functions to inhibit its enzymatic activity. Here, we attempt to further elucidate the role of LipY's PE domain in the regulation of its enzymatic activity. First, we established an improved purification method for several LipY variants using detergent micelles. We then used enzymatic assays to confirm that the PE domain down-regulates LipY activity. The PE domain must be attached to LipY in order to effectively inhibit it. Finally, we determined that full length LipY and the mature lipase lacking the PE domain (LipYΔPE) have similar melting temperatures. Based on our improved purification strategy and activity-based approach, we concluded that LipY's PE domain down-regulates its enzymatic activity but does not impact the thermal stability of the enzyme.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.